ID A0A1Y2V0C9_9PEZI Unreviewed; 328 AA.
AC A0A1Y2V0C9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carbohydrate-binding module family 1 protein {ECO:0000313|EMBL:OTA89851.1};
GN ORFNames=M434DRAFT_34095 {ECO:0000313|EMBL:OTA89851.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA89851.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA89851.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA89851.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family.
CC {ECO:0000256|ARBA:ARBA00009585}.
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DR EMBL; KZ112527; OTA89851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2V0C9; -.
DR STRING; 1001938.A0A1Y2V0C9; -.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd21175; LPMO_AA9; 1.
DR Gene3D; 2.70.50.70; -; 1.
DR InterPro; IPR005103; AA9.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR PANTHER; PTHR33353:SF9; ENDOGLUCANASE II; 1.
DR PANTHER; PTHR33353; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12560)-RELATED; 1.
DR Pfam; PF03443; AA9; 1.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..328
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012689039"
FT DOMAIN 293..328
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 328 AA; 33191 MW; 8A5893AC2C46AC0B CRC64;
MKSTIWATVA ALATKVASHA TFQDLWVNGV DMITTCARLP LSNSPVTDVT SKDIACNVGT
KPVSGKCSIA AGSIATVELK QQPGDRSCAS EAIGGAHYGP VQVYMASVAD SSSADGSSAS
WFKVFADTWE KNPSGSSGDD DYWGTKDINT CCGHMNVKIP SDLAPGDYLL RAEALALHTA
GQSGGAQFYM TCFQLTVTGG GSAKPAGVSL PGAYKASDPG ILVNIHAPLS TYIAPGPTVY
SGGSTKKAGS PCNGCESTCT AGKAPSTATG TSTPTQVVTL TTTAASPTGT SGCSVAIYGQ
CGGTGFSGCT TCAQGNCKKL NDYYSQCS
//
